Heme and FLVCR-related transporter families SLC48 and SLC49
Open accessAbstract
Heme is critical for a variety of cellular processes, but excess intracellular heme may result in oxidative stress and membrane injury. Feline leukemia virus subgroup C receptor (FLVCR1), a member of the SLC49 family of four paralogous genes, is a cell surface heme exporter, essential for erythropoiesis and systemic iron homeostasis. Disruption of FLVCR1 function blocks development of erythroid progenitors, likely due to heme toxicity. Mutations of SLC49A1 encoding FLVCR1 are noted in patients with a rare neurodegenerative disorder: posterior column ataxia with retinitis pigmentosa. FLVCR2 is highly homologous to FLVCR1 and may function as a cellular heme importer. Mutations of SLC49A2 encoding FLVCR2 are observed in Fowler syndrome, a rare proliferative vascular disorder of the brain. The functions of the remaining members of the SLC49 family, MFSD7 and DIRC2 (encoded by the SLC49A3 and SLC49A4 genes), are unknown, although the latter is implicated in hereditary renal carcinomas. SLC48A1 (heme responsive gene-1, HRG-1), the sole member of the SLC48 family, is associated with the endosome and appears to transport heme from the endosome into the cytosol.
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Absorption of heme iron is more effective but remains incompletely understood, although it appears to involve transporters of the SLC48 and SLC49 families.
“The absorption of HI is more effective but remains incompletely understood although it appears to involve transporters of the SLC48 (for solute carrier-48) and SLC49 families (Khan and Quigley, 2013).”
From Iron in infection and immunity (2020) · cites this paper as Khan and Quigley, 2013
The Therapeutic potential section says that most iron absorbed in Western diets is heme and that the small-intestinal heme importer remains to be identified. It presents the SLC49 transporter FLVCR2 as a possible importer needing further study, while the SLC48 Family—Conclusions section describes SLC48A1 primarily as an endosomal heme transporter. The paper therefore supports the uncertainty and a possible SLC49 role, but does not establish that intestinal heme absorption involves both families. (LLM, conf=0.86)
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Cites
[1] Role of free radicals and catalytic metal ions in human disease: An overview
Halliwell, B., & Gutteridge, J. M. C. (1990) · Methods in Enzymology · doi:10.1016/0076-6879(90)86093-b · Cited by 4,994 · see citing works
Cloning and characterization of a mammalian proton-coupled metal-ion transporter
Gunshin, H., Mackenzie, B., Berger, U. V., Gunshin, Y., Romero, M. F., Boron, W. F., Nussberger, S., Gollan, J. L., & Hediger, M. A. (1997) · Nature · doi:10.1038/41343 · Cited by 3,166 · see citing works
Pao, S. S., Paulsen, I. T., & Saier, M. H. (1998) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.62.1.1-34.1998 · Cited by 2,297 · see citing works
Vacuolar ATPases: rotary proton pumps in physiology and pathophysiology
Forgac, M. D. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2272 · Cited by 1,626 · see citing works
Microcytic anaemia mice have a mutation in Nramp2, a candidate iron transporter gene
Fleming, M. D., Trenor, C. C., Su, M. A., Foernzler, D., Beier, D. R., Dietrich, W. F., & Andrews, N. C. (1997) · Nature Genetics · doi:10.1038/ng0897-383 · Cited by 1,159 · see citing works
Proteolysis: from the lysosome to ubiquitin and the proteasome
Ciechanover, A. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1552 · Cited by 1,133 · see citing works
The Transporter Classification Database (TCDB): recent advances
Saier, M. H., Reddy, V. S., Tsu, B. V., Ahmed, M. S., Li, C., & Moreno‐Hagelsieb, G. (2015) · Nucleic Acids Research · doi:10.1093/nar/gkv1103 · Cited by 989 · see citing works
Qiu, A., Jansen, M., Sakaris, A., Min, S. H., Chattopadhyay, S., Tsai, E., Sandoval, C., Zhao, R., Akabas, M. H., & Goldman, I. D. (2006) · Cell · doi:10.1016/j.cell.2006.09.041 · Cited by 847 · see citing works
The heme synthesis and degradation pathways: role in oxidant sensitivity
Ryter, S. W., & Tyrrell, R. M. (2000) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(99)00223-3 · Cited by 822 · see citing works
The gene encoding ribosomal protein S19 is mutated in Diamond-Blackfan anaemia
Draptchinskaia, N., Gustavsson, P., Andersson, B., Pettersson, M., Willig, T.-N., Dianzani, I., Ball, S., Tchernia, G., Klar, J., Matsson, H., et al. (1999) · Nature Genetics · doi:10.1038/5951 · Cited by 795 · see citing works
Identification of an Intestinal Heme Transporter
Shayeghi, M., Latunde-Dada, G. O., Oakhill, J. S., Laftah, A. H., Takeuchi, K., Halliday, N., Khan, Y., Warley, A., McCann, F. E., Hider, R. C., et al. (2005) · Cell · doi:10.1016/j.cell.2005.06.025 · Cited by 755 · see citing works
Ponka, P. (1997) · Blood · doi:10.1182/blood.v89.1.1 · Cited by 544 · see citing works
Ogawa, K., Sun, J., Taketani, S., Nakajima, O., Nishitani, C., Sassa, S., Hayashi, N., Yamamoto, M., Shibahara, S., Fujita, H., et al. (2001) · The EMBO Journal · doi:10.1093/emboj/20.11.2835 · Cited by 532 · see citing works
Hulo, N., Bairoch, A., Bulliard, V., Cerutti, L., Cuche, B., de Castro, E., Lachaize, C., Langendijk-Genevaux, P. S., & Sigrist, C. J. A. (2007) · Nucleic Acids Research · doi:10.1093/nar/gkm977 · Cited by 500 · see citing works
Identification of a Human Heme Exporter that Is Essential for Erythropoiesis
Quigley, J. G., Yang, Z., Worthington, M., Phillips, J. D., Sabo, K. M., Sabath, D. E., Berg, C. L., Sassa, S., Wood, B. L., & Abkowitz, J. L. (2004) · Cell · doi:10.1016/j.cell.2004.08.014 · Cited by 423 · see citing works
Self-citationThe Transporter Classification Database: recent advances
Saier, M. H., Yen, M. R., Noto, K., Tamang, D. G., & Elkan, C. (2008) · Nucleic Acids Research · doi:10.1093/nar/gkn862 · Cited by 414 · see citing works
A Heme Export Protein Is Required for Red Blood Cell Differentiation and Iron Homeostasis
Keel, S. B., Doty, R. T., Yang, Z., Quigley, J. G., Chen, J., Knoblaugh, S., Kingsley, P. D., De Domenico, I., Vaughn, M. B., Kaplan, J., et al. (2008) · Science · doi:10.1126/science.1151133 · Cited by 404 · see citing works
Self-citationSun, J., Brand, M., Zenke, Y., Tashiro, S., Groudine, M., & Igarashi, K. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0308083100 · Cited by 364 · see citing works
Chimeric transcript discovery by paired-end transcriptome sequencing
Maher, C. A., Palanisamy, N., Brenner, J. C., Cao, X., Kalyana-Sundaram, S., Luo, S., Khrebtukova, I., Barrette, T. R., Grasso, C., Yu, J., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0904720106 · Cited by 339 · see citing works
Contributions of heme and nonheme iron to human nutrition
Carpenter, C. E., & Mahoney, A. W. (1992) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408399209527576 · Cited by 317 · see citing works
Haem homeostasis is regulated by the conserved and concerted functions of HRG-1 proteins
Rajagopal, A., Rao, A. U., Amigo, J., Tian, M., Upadhyay, S. K., Hall, C., Uhm, S., Mathew, M. K., Fleming, M. D., Paw, B. H., et al. (2008) · Nature · doi:10.1038/nature06934 · Cited by 316 · see citing works
The eIF‐2α kinases and the control of protein synthesis 1
de Haro, C., Méndez, R., & Santoyo‐López, J. (1996) · The FASEB Journal · doi:10.1096/fasebj.10.12.8903508 · Cited by 298 · see citing works
Heme is involved in microRNA processing
Faller, M., Matsunaga, M., Yin, S., Loo, J. A., & Guo, F. (2007) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1182 · Cited by 295 · see citing works
Danilova, N., Sakamoto, K. M., & Lin, S. L. (2008) · Blood · doi:10.1182/blood-2008-01-132290 · Cited by 291 · see citing works
Regulation by Heme of Mitochondrial Protein Transport Through a Conserved Amino Acid Motif
Lathrop, J. T., & Timko, M. P. (1993) · Science · doi:10.1126/science.8424176 · Cited by 282 · see citing works
Cyclic changes in metabolic state during the life of a yeast cell
Tu, B. P., Mohler, R. E., Liu, J. C., Dombek, K. M., Young, E. T., Synovec, R. E., & McKnight, S. L. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0708365104 · Cited by 260 · see citing works
Lack of heme synthesis in a free-living eukaryote
Rao, A. U., Carta, L. K., Lesuisse, E., & Hamza, I. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0500877102 · Cited by 241 · see citing works
Transfer of Heme from Ferrihemoglobin and Ferrihemoglobin Isolated Chains to Hemopexin
Hrkal, Z., Vodrážka, Z., & Kalousek, I. (1974) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1974.tb03386.x · Cited by 219 · see citing works
Trafficking of Heme and Porphyrins in Metazoa
Severance, S., & Hamza, I. (2009) · Chemical Reviews · doi:10.1021/cr9001116 · Cited by 209 · see citing works
The Association Rate Constant for Heme Binding to Globin Is Independent of Protein Structure
Hargrove, M. S., Barrick, D., & Olson, J. S. (1996) · Biochemistry · doi:10.1021/bi960371l · Cited by 209 · see citing works
Diamond-Blackfan Anemia: Diagnosis, Treatment, and Molecular Pathogenesis
Lipton, J. M. M., & Ellis, S. R. (2009) · Hematology/Oncology Clinics of North America · doi:10.1016/j.hoc.2009.01.004 · Cited by 208 · see citing works
Control of intracellular heme levels: Heme transporters and heme oxygenases
Khan, A., & Quigley, J. G. (2011) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2011.01.008 · Cited by 191 · see citing works
Self-citationWarnatz, H.-J., Schmidt, D., Manke, T., Piccini, I., Sultan, M., Borodina, T. A., Balzereit, D., Wruck, W., Солдатов, А. В., Vingron, M., et al. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.220178 · Cited by 189 · see citing works
Qi, Z., Hamza, I., & O’Brian, M. R. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.23.13056 · Cited by 170 · see citing works
Jaako, P., Flygare, J., Olsson, K., Quéré, R., Ehinger, M., Henson, A. L., Ellis, S. R., Schambach, A., Baum, C., Richter, J., et al. (2011) · Blood · doi:10.1182/blood-2011-08-371963 · Cited by 146 · see citing works
Why Heme Needs to Be Degraded to Iron, Biliverdin IXα, and Carbon Monoxide?
Sassa, S. (2004) · Antioxidants and Redox Signaling · doi:10.1089/ars.2004.6.819 · Cited by 145 · see citing works
Ribosomal protein gene deletions in Diamond-Blackfan anemia
Farrar, J. E., Vlachos, A., Atsidaftos, E., Carlson-Donohoe, H., Markello, T. C., Arceci, R. J., Ellis, S. R., Lipton, J. M. M., & Bodine, D. M. (2011) · Blood · doi:10.1182/blood-2011-08-375170 · Cited by 142 · see citing works
Hartmann, L. C., Lu, K. H., Linette, G. P., Cliby, W. A., Kalli, K. R., Gershenson, D., Bast, R. C., Stec, J., Iartchouk, N., Smith, D. I., et al. (2005) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-04-1673 · Cited by 141 · see citing works
Quigley, J. G., Burns, C. C., Anderson, M. M., Lynch, E. D., Sabo, K. M., Overbaugh, J. M., & Abkowitz, J. L. (2000) · Blood · doi:10.1182/blood.v95.3.1093.003k01_1093_1099 · Cited by 139 · see citing works
Self-citationvan Ham, M., & Hendriks, W. J. A. J. (2003) · Molecular Biology Reports · doi:10.1023/a:1023941703493 · Cited by 137 · see citing works
Tailor, C. S., Willett, B. J., & Kabat, D. (1999) · Journal of Virology · doi:10.1128/jvi.73.8.6500-6505.1999 · Cited by 137 · see citing works
The Fowler Syndrome-Associated Protein FLVCR2 Is an Importer of Heme
Duffy, S. P., Shing, J. C., Saraon, P., Berger, L., Eiden, M. V., Wilde, A., & Tailor, C. S. (2010) · Molecular and Cellular Biology · doi:10.1128/mcb.00690-10 · Cited by 130 · see citing works
Transport Protein Trafficking in Polarized Cells
Muth, T. R., & Caplan, M. J. (2003) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.19.110701.161425 · Cited by 122 · see citing works
Haem, haem oxygenase and ferritin in vascular endothelial cell injury
Balla, J. (2003) · Nephrology Dialysis Transplantation · doi:10.1093/ndt/gfg1034 · Cited by 120 · see citing works
Watanabe‐Matsui, M., Muto, A., Matsui, T., Itoh‐Nakadai, A., Nakajima, O., Murayama, K., Yamamoto, M. P., Ikeda‐Saito, M., & Igarashi, K. (2011) · Blood · doi:10.1182/blood-2010-07-296483 · Cited by 110 · see citing works
Mutations in FLVCR1 Cause Posterior Column Ataxia and Retinitis Pigmentosa
Rajadhyaksha, A. M., Elemento, O., Puffenberger, E. G., Schierberl, K. C., Xiang, J., Putorti, M. L., Berciano, J., Poulin, C., Brais, B., Michaelides, M., et al. (2010) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2010.10.013 · Cited by 108 · see citing works
Transmembrane heme delivery systems
Goldman, B. S., Beck, D. L., Monika, E. M., & Kranz, R. G. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.9.5003 · Cited by 106 · see citing works
Devlin, E. E., DaCosta, L., Mohandas, N., Elliott, G., & Bodine, D. M. (2010) · Blood · doi:10.1182/blood-2010-03-275776 · Cited by 97 · see citing works
Deniau, C., Gilli, R. M., Izadi‐Pruneyre, N., Létoffé, S., Delepierre, M., Wandersman, C., Briand, C. M., & Lecroisey, A. (2003) · Biochemistry · doi:10.1021/bi030015k · Cited by 92 · see citing works
Selective effect of feline leukaemia virus on early erythroid precursors
Onions, D. E., Jarrett, O., Testa, N. G., Frassoni, F., & Tóth, S. (1982) · Nature · doi:10.1038/296156a0 · Cited by 92 · see citing works
Transmembrane movement of heme.
Light, W. R., & Olson, J. S. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)55443-0 · Cited by 89 · see citing works
Yang, Z., Philips, J. D., Doty, R. T., Giraudi, P. J., Ostrow, J. D., Tiribelli, C., Smith, A., & Abkowitz, J. L. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.119131 · Cited by 87 · see citing works
Constitutive cycling: A general mechanism to regulate cell surface proteins
Royle, S., & Murrell‐Lagnado, R. D. (2002) · BioEssays · doi:10.1002/bies.10200 · Cited by 86 · see citing works
Meyer, E., Ricketts, C. J., Morgan, N. V., Morris, M. R., Pasha, S. S., Tee, L. J., Rahman, F., Bazin, A., Bessières, B., Déchelotte, P., et al. (2010) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2010.02.004 · Cited by 83 · see citing works
Heme and non-heme iron transporters in non-polarized and polarized cells
Yanatori, I., Tabuchi, M., Kawai, Y., Yasui, Y., Akagi, R., & Kishi, F. (2010) · BMC Cell Biology · doi:10.1186/1471-2121-11-39 · Cited by 83 · see citing works
CcsBA is a cytochrome c synthetase that also functions in heme transport
Frawley, E. R., & Kranz, R. G. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0903132106 · Cited by 77 · see citing works
Intracellular Trafficking of Porphyrins
Hamza, I. (2006) · ACS Chemical Biology · doi:10.1021/cb600442b · Cited by 74 · see citing works
Role of PUG1 in Inducible Porphyrin and Heme Transport in Saccharomyces cerevisiae
Protchenko, O. V., Shakoury‐Elizeh, M., Keane, P., Storey, J., Androphy, R., & Philpott, C. C. (2008) · Eukaryotic Cell · doi:10.1128/ec.00414-07 · Cited by 67 · see citing works
O’Callaghan, K., Ayllón, V., O'Keeffe, J., Wang, Y., Cox, Ó. T., Loughran, G., Forgac, M. D., & O’Connor, R. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.063248 · Cited by 66 · see citing works
Topologically Conserved Residues Direct Heme Transport in HRG-1-related Proteins
Yuan, X., Protchenko, O. V., Philpott, C. C., & Hamza, I. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.326785 · Cited by 66 · see citing works
Rey, M. A., Duffy, S. P., Brown, J. K., Kennedy, J. A., Dick, J. E., Dror, Y., & Tailor, C. S. (2008) · Haematologica · doi:10.3324/haematol.13359 · Cited by 56 · see citing works
An oxygen-sensitive mechanism in regulation of epithelial sodium channel
Wang, S., Publicover, S. J., & Gu, Y. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0809100106 · Cited by 52 · see citing works
Diamond Blackfan Anemia at the Crossroad between Ribosome Biogenesis and Heme Metabolism
Chiabrando, D., & Tolosano, E. (2010) · Advances in Hematology · doi:10.1155/2010/790632 · Cited by 50 · see citing works
Ishiura, H., Fukuda, Y., Mitsui, J., et al. (2011) · Neurogenetics · doi:10.1007/s10048-010-0271-4 · Cited by 49 · see citing works
Crosby, J. S., Chefalo, P. J., Yeh, I. M., et al. (2000) · Blood · doi:10.1182/blood.v96.9.3241 · Cited by 46 · see citing works
Bodmer, D. (2002) · Human Molecular Genetics · doi:10.1093/hmg/11.6.641 · Cited by 46 · see citing works
Warren, M. J., & Smith, A. G. (2009) · Springer eBooks · doi:10.1007/978-0-387-78518-9 · Cited by 42 · see citing works
Abkowitz, J. L., Holly, R. D., & Grant, C. K. (1987) · Journal of Clinical Investigation · doi:10.1172/jci113160 · Cited by 42 · see citing works
Genome-Wide Analysis Reveals Novel Genes Essential for Heme Homeostasis in Caenorhabditis elegans
Severance, S., Rajagopal, A., Rao, A. U., Cerqueira, G., Mitreva, M., El-Sayed, N. M., Krause, M., & Hamza, I. (2010) · PLoS Genetics · doi:10.1371/journal.pgen.1001044 · Cited by 41 · see citing works
Létoffé, S., Debarbieux, L., Izadi‐Pruneyre, N., Delepelaire, P., & Wandersman, C. (2003) · Molecular Microbiology · doi:10.1046/j.1365-2958.2003.03686.x · Cited by 41 · see citing works
Ectopic localizations of Golgi glycosyltransferases
Berger, E. G. (2002) · Glycobiology · doi:10.1093/glycob/12.2.29r · Cited by 39 · see citing works
Risk of Ovarian Cancer and Inherited Variants in Relapse-Associated Genes
Peedicayil, A., Vierkant, R. A., Hartmann, L. C., et al. (2010) · PLoS ONE · doi:10.1371/journal.pone.0008884 · Cited by 39 · see citing works
Brown, J., Fung, C., & Tailor, C. S. (2006) · Journal of Virology · doi:10.1128/jvi.80.4.1742-1751.2006 · Cited by 38 · see citing works
Shalev, Z., Duffy, S. P., Adema, K. W., Prasad, R., Hussain, N., Willett, B. J., & Tailor, C. S. (2009) · Journal of Virology · doi:10.1128/jvi.02317-08 · Cited by 37 · see citing works
Ricchelli, F., Gobbo, S. D., Jori, G., et al. (1995) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1995.159_1.x · Cited by 35 · see citing works
Savalas, L. R. T., Gasnier, B., Daμμe, M., et al. (2011) · Biochemical Journal · doi:10.1042/bj20110166 · Cited by 34 · see citing works
Thomas, S., Encha‐Razavi, F., Devisme, L., Etchevers, H., Bessières, B., Goudefroye, G., Elkhartoufi, N., Pateau, E., Ichkou, A., Bonnière, M., et al. (2010) · Human Mutation · doi:10.1002/humu.21329 · Cited by 32 · see citing works
Pdz Adaptors: Their Regulation of Epithelial Transporters and Involvement in Human Diseases
Sugiura, T., Shimizu, T., Kijima, A., Minakata, S., & Kato, Y. (2011) · Journal of Pharmaceutical Sciences · doi:10.1002/jps.22575 · Cited by 31 · see citing works
Diamond-Blackfan anemia, ribosome and erythropoiesis
Costa, L. M. D., Moniz, H., Simansour, M., et al. (2010) · Transfusion Clinique et Biologique · doi:10.1016/j.tracli.2010.06.001 · Cited by 29 · see citing works
Investigation of a putative role for FLVCR, a cytoplasmic heme exporter, in Diamond-Blackfan anemia
Quigley, J. G., Gazda, H. T., Yang, Z., Ball, S. E., Sieff, C. A., & Abkowitz, J. L. (2005) · Blood Cells Molecules and Diseases · doi:10.1016/j.bcmd.2005.01.005 · Cited by 28 · see citing works
Self-citationBarmchi, M. P., Browne, K., Sturgeon, K., Jusiak, B., & Auld, V. J. (2010) · Journal of Cell Science · doi:10.1242/jcs.066605 · Cited by 27 · see citing works
Lucas, M., Seidel, N., Porada, C., Quigley, J. G., Anderson, S., Malech, H., Abkowitz, J., Zanjani, E., & Bodine, D. (2005) · Blood · doi:10.1182/blood-2004-11-4491 · Cited by 27 · see citing works
Self-citationLipovich, L., Hughes, A. L., King, M., Abkowitz, J. L., & Quigley, J. G. (2002) · Gene · doi:10.1016/s0378-1119(02)00457-2 · Cited by 25 · see citing works
Self-citationBrasier, G., Tikellis, C., Xuereb, L., Craigie, J., CASLEY, D. J., Kovács, C. S., Fudge, N. J., Kalnins, R. M., Cooper, M. E., & Wookey, P. J. (2003) · Experimental Cell Research · doi:10.1016/j.yexcr.2003.10.002 · Cited by 25 · see citing works
A Novel Heme-responsive Element Mediates Transcriptional Regulation in Caenorhabditis elegans
Sinclair, J. W., & Hamza, I. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.167619 · Cited by 25 · see citing works
Bessières, B., Foliguet, B., Devisme, L., Lœuillet, L., Marcorelles, P., Bonnière, M., Laquerrière, A., Fallet‐Bianco, C., Martinovic, J., Zrelli, S., et al. (2009) · European Journal of Medical Genetics · doi:10.1016/j.ejmg.2009.07.006 · Cited by 22 · see citing works
Congenital Hydranencephalic-Hydrocephalic Syndrome Associated With Mitochondrial Dysfunction
Gago, M. C., Alonso, A., Pintos-Martínez, E., et al. (1999) · Journal of Child Neurology · doi:10.1177/088307389901400213 · Cited by 22 · see citing works
Imaizumi, T., Kay, S. A., & Schroeder, J. I. (2007) · Science · doi:10.1126/science.1151360 · Cited by 21 · see citing works
Polarisation, key to good localisation
van Beest, M., Robben, J. H., Savelkoul, P. J. M., et al. (2006) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2006.03.007 · Cited by 19 · see citing works
An All-Feline Retroviral Packaging System for Transduction of Human Cells
Doty, R. T., Sabo, K. M., Chen, J., Miller, A. D., & Abkowitz, J. L. (2010) · Human Gene Therapy · doi:10.1089/hum.2010.032 · Cited by 7 · see citing works
Heme Transport and Incorporation into Proteins
Thöny‐Meyer, L. (2009) · Springer eBooks · doi:10.1007/978-0-387-78518-9_9 · Cited by 4 · see citing works
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Research works printed but not linked: 1
- Aicardi J Diseases of the nervous system in childhood / Jean Aicardi; with contributions from Martin Bax, Christopher Gillberg, Helene Ogier 1992 Mac Keith Press London
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Nairz, M., & Weiss, G. (2020) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2020.100864 · Cited by 359 · see citing works
Iron and innate antimicrobial immunity-depriving the pathogen, defending the host
Nairz, M., Dichtl, S., Schroll, A., Haschka, D., Tymoszuk, P., Theurl, I., & Weiss, G. (2018) · Journal of Trace Elements in Medicine and Biology · doi:10.1016/j.jtemb.2018.03.007 · Cited by 123 · see citing works
- Authors
- Khan, A. A., & Quigley, J. G.
- Affiliations
- University of Illinois Chicago (US)
- Corresponding author
- Quigley, John G.
- Venue
- Molecular Aspects of Medicine
- Publisher
- Elsevier BV
- Published
- 2013-04
- Volume
- 34
- Issue
- 2-3
- Pages
- 669-682
- ISSN
- 0098-2997 (ISSN-L)
- PMC
- PMC3602793
- OpenAlex
- W2024199244
- Cited by
- 105
- References
- 92
- Citations by year
- 2026: 5 · 2025: 6 · 2024: 5 · 2023: 9 · 2022: 10 · 2021: 8 · 2020: 20 · 2019: 4 · 2018: 7 · 2017: 8 · 2016: 4 · 2015: 8 · 2014: 8 · 2013: 3
- FWCI
- 1.17
- Type
- journal article
- Language
- en
- Open access
- green
- europepmc.org
- Locations
- Molecular Aspects of Medicine (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institutes of Health
- National Heart, Lung, and Blood Institute (K08HL087842)
- Topics
- Health Sciences › Medicine › Hematology › Iron Metabolism and Disorders
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Hemoglobin structure and function
- Health Sciences › Medicine › Oncology › Drug Transport and Resistance Mechanisms
- Keywords
- heme transport, FLVCR1, iron homeostasis, erythropoiesis, Fowler syndrome, heme toxicity, oxidative stress
- MeSH terms
- Cerebrovascular Disorders, Gene Expression Regulation, Multigene Family, Heme, Hemeproteins, Homeostasis, Humans, Iron, Models, Molecular, Mutation, Receptors, Virus, Endosomes, Erythroid Precursor Cells, Membrane Transport Proteins
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